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Cold Spring Harbor Perspectives in Biology (1)
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The Journal of Cell Biology (1)
Bennett, Vann (3)
Healy, Jane (2)
Healy, Jane A. (1)
Kline, Crystal F. (1)
Kranias, Evangelia G. (1)
Mohler, Peter J. (1)
Puca, Annibale A. (1)
Rand Allingham, R. (1)
Rockman, Howard A. (1)
Xue, Hui (1)
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Membrane Domains Based on Ankyrin and Spectrin Associated with Cell–Cell Interactions
Cold Spring Harbor Perspectives in Biology
Nodes of Ranvier and axon initial segments of myelinated nerves, sites of cell–cell contact in early embryos and epithelial cells, and neuromuscular junctions of skeletal muscle all perform physiological functions that depend on clustering of functionally related but structurally diverse ion transporters and cell adhesion molecules within microdomains of the plasma membrane. These specialized cell surface domains appeared at different times in metazoan evolution, involve a variety of cell types, and are populated by distinct membrane-spanning proteins. Nevertheless, recent work has shown that these domains all share on their cytoplasmic surfaces a membrane skeleton comprised of members of the ankyrin and spectrin families. This review will summarize basic features of ankyrins and spectrins, and will discuss emerging evidence that these proteins are key players in a conserved mechanism responsible for assembly and maintenance of physiologically important domains on the surfaces of diverse cells.
Ankyrins and spectrins form a “skeleton” beneath the plasma membrane, clustering ion channels and other proteins together to generate distinct microdomains.
Being there: cellular targeting of voltage-gated sodium channels in the heart
The Journal of Cell Biology
Voltage-gated sodium (Nav) channels in cardiomyocytes are localized in specialized membrane domains that optimize their functions in propagating action potentials across cell junctions and in stimulating voltage-gated calcium channels located in T tubules. Mutation of the ankyrin-binding site of Nav1.5, the principal Nav channel in the heart, was previously known to cause cardiac arrhythmia and the retention of Nav1.5 in an intracellular compartment in cardiomyocytes. Conclusive evidence is now provided that direct interaction between Nav1.5 and ankyrin-G is necessary for the expression of Nav1.5 at the cardiomyocyte cell surface.
Ankyrin-B Syndrome: Enhanced Cardiac Function Balanced by Risk of Cardiac Death and Premature Senescence
Mohler, Peter J.
Puca, Annibale A.
Kline, Crystal F.
Rand Allingham, R.
Kranias, Evangelia G.
Rockman, Howard A.
Here we report the unexpected finding that specific human ANK2 variants represent a new example of balanced human variants. The prevalence of certain ANK2 (encodes ankyrin-B) variants range from 2 percent of European individuals to 8 percent in individuals from West Africa. Ankyrin-B variants associated with severe human arrhythmia phenotypes (eg E1425G, V1516D, R1788W) were rare in the general population. Variants associated with less severe clinical and in vitro phenotypes were unexpectedly common. Studies with the ankyrin-B+/− mouse reveal both benefits of enhanced cardiac contractility, as well as costs in earlier senescence and reduced lifespan. Together these findings suggest a constellation of traits that we term “ankyrin-B syndrome”, which may contribute to both aging-related disorders and enhanced cardiac function.
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